Regulation of trehalase expression inhibits apoptosis in diapause cysts of Artemia

Author:

Yang Fan1,Chen Su2,Dai Zhong-Min3,Chen Dian-Fu1,Duan Ru-Bing1,Wang Hong-Liang1,Jia Sheng-Nan1,Yang Wei-Jun1

Affiliation:

1. Key Laboratory of Conservation Biology for Endangered Wildlife of the Ministry of Education and College of Life Sciences, Zijingang Campus, Zhejiang University, Hangzhou 310058, Zhejiang, People's Republic of China

2. Hangzhou Wahaha Technology Co. Ltd. Street 14, Xiasha Economic and Technological Development Zone, Hangzhou 310018, Zhejiang, People's Republic of China

3. Institute of Developmental and Regenerative Biology, College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou 310036, Zhejiang, People's Republic of China

Abstract

Trehalase, which specifically hydrolyses trehalose into glucose, plays an important role in the metabolism of trehalose. Large amounts of trehalose are stored in the diapause encysted embryos (cysts) of Artemia, which are not only vital to their extraordinary stress resistance, but also provide a source of energy for development after diapause is terminated. In the present study, a mechanism for the transcriptional regulation of trehalase was described in Artemia parthenogenetica. A trehalase-associated protein (ArTAP) was identified in Artemia-producing diapause cysts. ArTAP was found to be expressed only in diapause-destined embryos. Further analyses revealed that ArTAP can bind to a specific intronic segment of a trehalase gene. Knockdown of ArTAP by RNAi resulted in the release of cysts with coarse shells in which two chitin-binding proteins were missing. Western blotting showed that the level of trehalase was increased and apoptosis was induced in these ArTAP-knockdown cysts compared with controls. Taken together, these results show that ArTAP is a key regulator of trehalase expression which, in turn, plays an important role in trehalose metabolism during the formation of diapause cysts.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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